1EPF


Conserved Protein Domain Family
Ig1_NCAM-1

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cd05865: Ig1_NCAM-1 
Click on image for an interactive view with Cn3D
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1
Ig1_NCAM-1: first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.
Statistics
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PSSM-Id: 143273
View PSSM: cd05865
Aligned: 4 rows
Threshold Bit Score: 181.374
Threshold Setting Gi: 127855
Created: 11-Jan-2008
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interface
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:
  • Structure:1EPF_A, rat neural cell adhesion molecule (NCAM) dimer showing Ig1-Ig2 dimer interface, contacts based on 3.5 A distance.
    View structure with Cn3D
  • Comment:Dimerization mediates cell-cell recognition and adhesion.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                        # ##                                                             
1EPF_A          3 LQVDIVPSQGEISVGESKFFLCQVAGdakdKDISWFSPNGEKlspnqqrISVVWNDDDSSTLTIYNANIDDAGIYKCVVT 82
gi 127855      20 LEVNIVPDQGEISLGESKFFLCQVSGe--aTDISWYSPTGEKlvt-qqqISVVRSDDYTSTLTIYNASSQDAGIYKCVAS 96
gi 2851523     20 LQVDIVPSQGEISVGESKFFLCQVAGeakyKDISWFSPNGEKltpnqqrISVVRNDDFSSTLTIYNANIDDAGIYKCVVS 99
gi 119587605   20 LQVDIVPSQGEISVGESKFFLCQVAGdakdKDISWFSPNGEKltpnqqrISVVWNDDSSSTLTIYNANIDDAGIYKCVVT 99
                          90
                  ....*....|....*.
Feature 1                         
1EPF_A         83 aedgTQSEATVNVKIF 98
gi 127855      97 neaeGESEGTVNLKIY 112
gi 2851523    100 sveeGDSEATVNVKIF 115
gi 119587605  100 gedgSESEATVNVKIF 115

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